ArticleScientific reports2020
A bispecific IgG format containing four independent antigen binding sites.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Target-mediated drug disposition model for drugs with N > 2 binding sites that bind to a target with one binding site.Journal of pharmacokinetics and pharmacodynamics · 2024Article
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- Bispecific Antibody Detection Using Antigen-Conjugated Synthetic Nucleic Acid Strands.ACS sensors · 2023Article
- Fully synthetic platform to rapidly generate tetravalent bispecific nanobody-based immunoglobulins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dual-target Bridging ELISA for Bispecific Antibodies.Bio-protocol · 2022Article
- A Generic Strategy to Generate Bifunctional Two-in-One Antibodies by Chicken Immunization.Frontiers in immunology · 2022Article
- Bioassay Development for Bispecific Antibodies-Challenges and Opportunities.International journal of molecular sciences · 2021Review
- DutaFabs are engineered therapeutic Fab fragments that can bind two targets simultaneously.Nature communications · 2021Article
- Format and geometries matter: Structure-based design defines the functionality of bispecific antibodies.Computational and structural biotechnology journal · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bispecific antibodies come in many different formats, including the particularly interesting two-in-one antibodies, where one conventional IgG binds two different antigens. The IgG format allows these antibodies to mediate Fc-related functionality, and their wild-type structure ensures low immunogenicity and enables standard methods to be used for development. It is however difficult, time-consuming and costly to generate two-in-one antibodies. Herein we demonstrate a new approach to create a similar type of antibody by combining two different variable heavy (VH) domains in each Fab arm of an IgG, a tetra-VH IgG format. The VHs are used as building blocks, where one VH is placed at its usual position, and the second VH replaces the variable light (VL) domain in a conventional IgG. VH domains, binding several different types of antigens, were discovered and could be rearranged in any combination, offering a convenient "plug and play" format. The tetra-VH IgGs were found to be functionally tetravalent, binding two antigens on each arm of the IgG molecule simultaneously. This offers a new strategy to also create monospecific, tetravalent IgGs that, depending on antigen architecture and mode-of-action, may have enhanced efficacy compared to traditional bivalent antibodies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.